ID   PRXC_KITAU              Reviewed;         278 AA.
AC   O31168;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   27-MAR-2024, entry version 101.
DE   RecName: Full=Non-heme chloroperoxidase;
DE            EC=1.11.1.-;
DE   AltName: Full=Chloride peroxidase;
DE   AltName: Full=Chloroperoxidase T;
DE            Short=CPO-T;
GN   Name=cpo; Synonyms=cpoT;
OS   Kitasatospora aureofaciens (Streptomyces aureofaciens).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Kitasatospora.
OX   NCBI_TaxID=1894;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Tu24;
RA   Pelletier I., Altenbuchner J., van Pee K.-H.;
RL   Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS).
RC   STRAIN=Tu24;
RX   PubMed=9642069; DOI=10.1006/jmbi.1998.1802;
RA   Hofmann B., Tolzer S., Pelletier I., Altenbuchner J., van Pee K.-H.,
RA   Hecht H.-J.;
RT   "Structural investigation of the cofactor-free chloroperoxidases.";
RL   J. Mol. Biol. 279:889-900(1998).
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Bacterial non-heme
CC       haloperoxidase / perhydrolase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF031242; AAB86626.1; -; Genomic_DNA.
DR   RefSeq; WP_033354363.1; NZ_JNWR01000048.1.
DR   PDB; 1A7U; X-ray; 1.75 A; A/B=2-278.
DR   PDB; 1A8U; X-ray; 1.60 A; A/B=2-278.
DR   PDBsum; 1A7U; -.
DR   PDBsum; 1A8U; -.
DR   AlphaFoldDB; O31168; -.
DR   SMR; O31168; -.
DR   DrugBank; DB03793; Benzoic acid.
DR   ESTHER; strau-cpoT; Haloperoxidase.
DR   MEROPS; S33.991; -.
DR   PeroxiBase; 5908; STaHalNPrx02.
DR   EvolutionaryTrace; O31168; -.
DR   GO; GO:0016691; F:chloride peroxidase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR000639; Epox_hydrolase-like.
DR   PANTHER; PTHR43433; HYDROLASE, ALPHA/BETA FOLD FAMILY PROTEIN; 1.
DR   PANTHER; PTHR43433:SF3; NON-HEME CHLOROPEROXIDASE-RELATED; 1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   PRINTS; PR00111; ABHYDROLASE.
DR   PRINTS; PR00412; EPOXHYDRLASE.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Chloride; Oxidoreductase; Peroxidase.
FT   CHAIN           1..278
FT                   /note="Non-heme chloroperoxidase"
FT                   /id="PRO_0000207062"
FT   DOMAIN          26..264
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        99
FT                   /evidence="ECO:0000250|UniProtKB:P22862"
FT   ACT_SITE        229
FT                   /evidence="ECO:0000250|UniProtKB:P22862"
FT   ACT_SITE        258
FT                   /evidence="ECO:0000250|UniProtKB:P22862"
FT   STRAND          3..9
FT                   /evidence="ECO:0007829|PDB:1A8U"
FT   STRAND          12..22
FT                   /evidence="ECO:0007829|PDB:1A8U"
FT   STRAND          24..30
FT                   /evidence="ECO:0007829|PDB:1A8U"
FT   HELIX           37..40
FT                   /evidence="ECO:0007829|PDB:1A8U"
FT   HELIX           41..49
FT                   /evidence="ECO:0007829|PDB:1A8U"
FT   STRAND          53..57
FT                   /evidence="ECO:0007829|PDB:1A8U"
FT   HELIX           74..88
FT                   /evidence="ECO:0007829|PDB:1A8U"
FT   STRAND          92..98
FT                   /evidence="ECO:0007829|PDB:1A8U"
FT   HELIX           100..112
FT                   /evidence="ECO:0007829|PDB:1A8U"
FT   STRAND          117..124
FT                   /evidence="ECO:0007829|PDB:1A8U"
FT   STRAND          139..141
FT                   /evidence="ECO:0007829|PDB:1A8U"
FT   HELIX           143..155
FT                   /evidence="ECO:0007829|PDB:1A8U"
FT   HELIX           157..168
FT                   /evidence="ECO:0007829|PDB:1A8U"
FT   HELIX           171..174
FT                   /evidence="ECO:0007829|PDB:1A8U"
FT   TURN            176..178
FT                   /evidence="ECO:0007829|PDB:1A8U"
FT   HELIX           181..193
FT                   /evidence="ECO:0007829|PDB:1A8U"
FT   HELIX           196..205
FT                   /evidence="ECO:0007829|PDB:1A8U"
FT   TURN            211..213
FT                   /evidence="ECO:0007829|PDB:1A8U"
FT   HELIX           214..216
FT                   /evidence="ECO:0007829|PDB:1A8U"
FT   STRAND          221..226
FT                   /evidence="ECO:0007829|PDB:1A8U"
FT   STRAND          230..232
FT                   /evidence="ECO:0007829|PDB:1A8U"
FT   HELIX           234..236
FT                   /evidence="ECO:0007829|PDB:1A8U"
FT   HELIX           238..244
FT                   /evidence="ECO:0007829|PDB:1A8U"
FT   STRAND          248..253
FT                   /evidence="ECO:0007829|PDB:1A8U"
FT   HELIX           260..263
FT                   /evidence="ECO:0007829|PDB:1A8U"
FT   HELIX           265..277
FT                   /evidence="ECO:0007829|PDB:1A8U"
SQ   SEQUENCE   278 AA;  30355 MW;  8C97A87251FBEDE5 CRC64;
     MPFITVGQEN STSIDLYYED HGAGQPVVLI HGFPLSGHSW ERQSAALLDA GYRVITYDRR
     GFGQSSQPTT GYDYDTFAAD LNTVLETLDL QDAVLVGFSM GTGEVARYVS SYGTARIAKV
     AFLASLEPFL LKTDDNPDGA APKEFFDGIV AAVKADRYAF YTGFFNDFYN LDENLGTRIS
     EEAVRNSWNT AASGGFFAAA AAPTTWYTDF RADIPRIDVP ALILHGTGDR TLPIENTARV
     FHKALPSAEY VEVEGAPHGL LWTHAEEVNT ALLAFLAK
//